000 01823 a2200493 4500
005 20250513150142.0
264 0 _c19981021
008 199810s 0 0 eng d
022 _a0961-8368
024 7 _a10.1002/pro.5560070705
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aSzpikowska, B K
245 0 0 _aMgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains.
_h[electronic resource]
260 _bProtein science : a publication of the Protein Society
_cJul 1998
300 _a1524-30 p.
_bdigital
500 _aPublication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.
650 0 4 _aAdenosine Triphosphate
_xanalogs & derivatives
650 0 4 _aAmino Acid Sequence
650 0 4 _aAnimals
650 0 4 _aArchaeal Proteins
_xchemistry
650 0 4 _aChaperonin 60
_xchemistry
650 0 4 _aChaperonin Containing TCP-1
650 0 4 _aChaperonins
_xchemistry
650 0 4 _aChromatography, High Pressure Liquid
650 0 4 _aCrystallization
650 0 4 _aElectrophoresis, Polyacrylamide Gel
650 0 4 _aMass Spectrometry
650 0 4 _aMice
650 0 4 _aModels, Molecular
650 0 4 _aMolecular Sequence Data
650 0 4 _aPeptide Mapping
650 0 4 _aProtein Conformation
_xdrug effects
650 0 4 _aRabbits
650 0 4 _aSequence Alignment
650 0 4 _aSequence Homology, Amino Acid
650 0 4 _aThermosomes
650 0 4 _aTime Factors
650 0 4 _aTrypsin
700 1 _aSwiderek, K M
700 1 _aSherman, M A
700 1 _aMas, M T
773 0 _tProtein science : a publication of the Protein Society
_gvol. 7
_gno. 7
_gp. 1524-30
856 4 0 _uhttps://doi.org/10.1002/pro.5560070705
_zAvailable from publisher's website
999 _c9650613
_d9650613